Protein profile

PA5187

acyl-CoA dehydrogenase

Genome: NC_002516.2

Gene: PA5187 Structure source: AlphaFold UniProt Q9HU02
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Amino acids 596
Annotations 3
Features 21
PDB binders 14
Druggability 0.236

Overview

Basic information about this protein and its source genome.

Accession
PA5187
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5187
Status
annotated
Amino acids
596
Structure source
AlphaFold
EC
1.3.99.41
GO
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
43.137
Human E-value
8.18e-06
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.236
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 2 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

2
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
158 284 FunFam G3DSA:2.40.110.10:FF:000031 Acyl-CoA dehydrogenase, putative
160 269 Pfam PF02770 Acyl-CoA dehydrogenase, middle domain
160 269 InterPro IPR006091 Acyl-CoA oxidase/dehydrogenase, middle domain
478 590 Pfam PF12806 Acetyl-CoA dehydrogenase C-terminal like
478 590 InterPro IPR025878 Acetyl-CoA dehydrogenase-like C-terminal domain
158 283 Gene3D G3DSA:2.40.110.10 -
158 283 InterPro IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
284 454 Gene3D G3DSA:1.20.140.10 -
279 451 Pfam PF00441 Acyl-CoA dehydrogenase, C-terminal domain
279 451 InterPro IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal
39 276 SUPERFAMILY SSF56645 Acyl-CoA dehydrogenase NM domain-like
39 276 InterPro IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
284 456 SUPERFAMILY SSF47203 Acyl-CoA dehydrogenase C-terminal domain-like
284 456 InterPro IPR036250 Acyl-CoA dehydrogenase-like, C-terminal
34 156 Gene3D G3DSA:1.10.540.10 -
34 156 InterPro IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
2 594 PANTHER PTHR42803 ACYL-COA DEHYDROGENASE
46 155 Pfam PF02771 Acyl-CoA dehydrogenase, N-terminal domain
46 155 InterPro IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal
2 26 Pfam PF12418 Acyl-CoA dehydrogenase N terminal
2 26 InterPro IPR020953 Acyl-CoA dehydrogenase, N-terminal, bacteria

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5187
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
2 0.236

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

64 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
6NA
6LQ0
Q3L887 116.2 Da LogP 1.65 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCC(=O)O
B3P
6IJC
A3SI50 282.3 Da LogP -4.01 TPSA 145.4 1 viol. ✓ Clean C(CNC(CO)(CO)CO)CNC(CO)(CO)CO
BUA
6LPY
Q3L887 88.1 Da LogP 0.87 TPSA 37.3 ✓ Ro5 ✓ Clean CCCC(=O)O
COS
5OL2
A0A031WJ47 799.6 Da LogP -1.02 TPSA 346.6 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
DAO
6LQ3
Q3L887 200.3 Da LogP 3.99 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCCCC(=O)O
DCR
6LQ6
Q3L887 312.5 Da LogP 7.11 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCC(=O)O
DKA
6LQ2
Q3L887 172.3 Da LogP 3.21 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCC(=O)O
EO3
6LQ8
Q3L887 340.6 Da LogP 7.89 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCCCC(=O)O
FDA
3PFD
G7CNE7 787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…
MYR
6LQ4
Q3L887 228.4 Da LogP 4.77 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCCCCCC(=O)O
OCA
6LQ1
Q3L887 144.2 Da LogP 2.43 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCC(=O)O
PLM
6KSB
Q3L887 256.4 Da LogP 5.55 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)O
ST9
6KSE
O53666 1034.0 Da LogP 4.93 TPSA 363.6 3 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C…
X90
6LQ7
Q3L887 270.5 Da LogP 5.94 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCCC(=O)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.